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Conserved domains on  [gi|121592322|gb|ABM63257|]
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ATP synthase F0 subunit 6 (mitochondrion) [Ailuropoda melanoleuca]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 4.87e-137

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 383.15  E-value: 4.87e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121592322 161 TANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 4.87e-137

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 383.15  E-value: 4.87e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121592322 161 TANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-225 8.93e-55

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 174.70  E-value: 8.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322    6 FASFTTPMMMGVPIVVLIIIFpsILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNLL 85
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFL--ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   86 GLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANIT 165
Cdd:TIGR01131  88 GLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANIS 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  166 AGHLLIHLIGGATLVLMNINPVTalITFIILILLTILELAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 168 AGHLLLTLLSGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 2.64e-42

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 140.61  E-value: 2.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  65 GQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121592322 145 ETISLFIQPVALAVRLTANITAGHLLIHLIGGATLVLMNInpvTALITFIILILLTILELAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 8.35e-41

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 138.39  E-value: 8.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   13 MMMGVPIVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLS-IHNYKGQTWALMLMSLILFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   89 PHSFTPTTQLSMNLGMAIPLWAGTVVMGFR-HKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 121592322  168 HLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 1.42e-26

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 101.69  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  19 IVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356    8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  99 SMNLGMAIPLWAGTVVMGFRHK-TKASLAHFLPQGTPlPLIPMLVIIETISLFIQPVALAVRLTANITAGHLLIHLIGGA 177
Cdd:COG0356   88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 121592322 178 TLVLMninpvTALITFIILILLTILELAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356  167 APFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 4.87e-137

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 383.15  E-value: 4.87e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121592322 161 TANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 2.34e-87

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 257.45  E-value: 2.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSP-NRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFI 79
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVR 159
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121592322 160 LTANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 1.73e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 247.96  E-value: 1.73e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSP-NRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFI 79
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPtNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVR 159
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121592322 160 LTANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 8.79e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 245.94  E-value: 8.79e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSP-NRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFI 79
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPtSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVR 159
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121592322 160 LTANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.63e-73

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 222.52  E-value: 1.63e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSP-NRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFI 79
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVR 159
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121592322 160 LTANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-225 8.93e-55

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 174.70  E-value: 8.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322    6 FASFTTPMMMGVPIVVLIIIFpsILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNLL 85
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFL--ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   86 GLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANIT 165
Cdd:TIGR01131  88 GLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANIS 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  166 AGHLLIHLIGGATLVLMNINPVTalITFIILILLTILELAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 168 AGHLLLTLLSGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 1.04e-45

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 151.47  E-value: 1.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIG 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121592322 161 TANITAGHLLIHLIGGatlVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLY 221
Cdd:MTH00157 161 AANMIAGHLLLTLLGN---TGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 1.76e-45

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 150.89  E-value: 1.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLIIIFPS--ILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILF 78
Cdd:MTH00035   3 INNSIFGQFSPDTILFIPLTLLSSVIALswLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAV 158
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121592322 159 RLTANITAGHLLIHLIGGATLVLMNiNPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 2.64e-42

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 140.61  E-value: 2.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  65 GQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121592322 145 ETISLFIQPVALAVRLTANITAGHLLIHLIGGATLVLMNInpvTALITFIILILLTILELAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 8.35e-41

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 138.39  E-value: 8.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   13 MMMGVPIVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLS-IHNYKGQTWALMLMSLILFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   89 PHSFTPTTQLSMNLGMAIPLWAGTVVMGFR-HKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 121592322  168 HLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 8.16e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 134.00  E-value: 8.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   1 MNENLFASFTTPMMMGVPIVVLI---IIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLIL 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALA 157
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121592322 158 VRLTANITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 13-224 4.26e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 131.91  E-value: 4.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  13 MMMGVPIVVLIIIFPSILFPSPNrlinnrLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNLLGLLPHSF 92
Cdd:MTH00173  22 LMWLLSLMSLFFFSSSVWVSSSN------LSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  93 TPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANITAGHLLIH 172
Cdd:MTH00173  96 SVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLT 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 121592322 173 LIGGA-TLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173 176 LIGNYlSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 5-224 5.77e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 116.29  E-value: 5.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   5 LFASFTTPMMMGVPIVVLIIIFPSilfpspNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNL 84
Cdd:MTH00172  14 LIGLTNSSIMMILVIIVVLLLFKG------IKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  85 LGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANI 164
Cdd:MTH00172  88 LGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322 165 TAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172 168 SAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 8-224 1.38e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 110.48  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   8 SFTTPMMMgvpiVVLIIIFPSILFPSpNRLINNRLATVQQwLIQLVSKYMLSIH-NYKGQTWALMLMSLILFIGSTNLLG 86
Cdd:MTH00175  27 TFTNSSMM----MVLAVIIFWLLLKG-DKLIPNRWQSIME-LIYLNIRSVVHDNlGKSGQKYFPFILSLFLFIAILNILG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  87 LLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANITA 166
Cdd:MTH00175 101 LFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISA 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 121592322 167 GHLLIHLIGGATL-VLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175 181 GHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 4-226 3.79e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 109.05  E-value: 3.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   4 NLFASFTTPMMMGVPIVVLIIIFPSILfpspnrLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTN 83
Cdd:MTH00005  15 SLFNNLSSTAFWAFNFSIILLLSSSFW------ITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  84 LLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTAN 163
Cdd:MTH00005  89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121592322 164 ITAGHLLIHLIGGATLVLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005 169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 1.42e-26

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 101.69  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  19 IVVLIIIFPSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356    8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  99 SMNLGMAIPLWAGTVVMGFRHK-TKASLAHFLPQGTPlPLIPMLVIIETISLFIQPVALAVRLTANITAGHLLIHLIGGA 177
Cdd:COG0356   88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 121592322 178 TLVLMninpvTALITFIILILLTILELAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356  167 APFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 8-224 3.29e-23

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 93.32  E-value: 3.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322   8 SFTTPMMMGVPIVVLIIIFpSILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNLLGL 87
Cdd:PRK05815  13 NFDSLLLSVLLGVLILLLF-ALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  88 LP-HSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKtkaSLAHFLPQGTPLPlIPMLVIIETISLFIQPVALAVRLTANITA 166
Cdd:PRK05815  92 IPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 121592322 167 GHLLIHLIGGatlvLMNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815 168 GELILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 1.06e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 81.91  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  64 KGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPLPLIPMLVI 143
Cdd:MTH00174  86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322 144 IETISLFIQPVALAVRLTANITAGHLLIHLIGGATLVLMNINP-VTALITFIILILLTILELAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGIlIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                 ..
gi 121592322 223 HD 224
Cdd:MTH00174 246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 2.43e-17

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 79.40  E-value: 2.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  72 LMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFR-HKTKASLAHfLPQGTPLPLIPMLVIIETISLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121592322 151 IQPVALAVRLTANITAGHLLIHLIGGATLVLmNINPVTALITFIILILLTILELAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVILSLIFISFIL-KSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 74-222 2.77e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 57.68  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASlaHFLPQGTPLPLIPM-LVIIETISLFIQ 152
Cdd:MTH00087  57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSELSR 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322 153 PVALAVRLTANITAGHLLIHLIGgatlvlmninpVTALITFIILILLTILELAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLN-----------FLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 13-222 5.14e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 55.28  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  13 MMMGVPIVVLIIIFPS--ILFPSPNRLINNRLATVQQWLIQLVSKYMLSIHNYKGQTWALMLMSLILFIGSTNLLGLLP- 89
Cdd:PRK13417 100 MMWIVAFFLFLIFIPAanIIAKNPLKVQSRFANTVEVFVNFLRKDIVDESMHGHGHSYYHYIFTLFFFILFCNLMGLVPs 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  90 ---------------------------HSF-------TPTTQLSMNLGMAIPLWAGTVVMGFRHKTKASLAHFLPQGTPL 135
Cdd:PRK13417 180 vgeltvvasdygglvalgvmdhtphalPTFakvwsgiTVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPL 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322 136 PLIPMLVIIETI-SLFIQPVALAVRLTANITAGHLLIHLIGGatLVLMNINPVTALITFIILILLTILELAVALIQAYVF 214
Cdd:PRK13417 260 LLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIF 337


                 ....*...
gi 121592322 215 TLLVSLYL 222
Cdd:PRK13417 338 VLLTSLFV 345
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 126-167 5.44e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.40  E-value: 5.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 121592322 126 AHFLPQGTPLPLIPMLVIIETISLFIQPVALAVRLTANITAG 167
Cdd:MTH00050  80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 71-222 6.46e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 36.64  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121592322  71 MLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVVMGFRHK-TKASLAHFLpqgTPLP-LIPMLVIIEtis 148
Cdd:PRK13420  77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYL---SPSPfLLPFHLISE--- 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121592322 149 lFIQPVALAVRLTANITAGHLlihligGATLVLMninpVTALITFIILILLTILElavALIQAYVFTLLVSLYL 222
Cdd:PRK13420 151 -ITRTLALAVRLFGNIMSLEL------AALLVLL----VAGFLVPVPILMLHIIE---ALVQAYIFGMLALIYI 210
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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